ID   A2BWA5_PROM5            Unreviewed;       545 AA.
AC   A2BWA5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=P9515_08591 {ECO:0000313|EMBL:ABM72066.1};
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167542 {ECO:0000313|EMBL:ABM72066.1, ECO:0000313|Proteomes:UP000001589};
RN   [1] {ECO:0000313|EMBL:ABM72066.1, ECO:0000313|Proteomes:UP000001589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515 {ECO:0000313|EMBL:ABM72066.1,
RC   ECO:0000313|Proteomes:UP000001589};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
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DR   EMBL; CP000552; ABM72066.1; -; Genomic_DNA.
DR   RefSeq; WP_011820171.1; NC_008817.1.
DR   AlphaFoldDB; A2BWA5; -.
DR   STRING; 167542.P9515_08591; -.
DR   GeneID; 60200735; -.
DR   KEGG; pmc:P9515_08591; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_005138_6_2_3; -.
DR   OrthoDB; 9767858at2; -.
DR   Proteomes; UP000001589; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07897; Adenylation_DNA_ligase_Bac1; 1.
DR   CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR04120; DNA_lig_bact; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABM72066.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          313..450
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   545 AA;  63999 MW;  8ED3D03554BD39E3 CRC64;
     MSLKKFSELY LDLDSCNSTN KKIEILNNYF SSNEDLENAW TIYLLTGKKN KRFISGSLLK
     TLFSEIYEYP LWLIDSCYLK VGDSSEVISL LLRNKIIGRN YKYQNISLNE LLNKFLPDLY
     ILKEEDKKLR LKEIWENIPK ENHLVINKIL TGTFRVGVSI GLITKSIAKL INLEEAIISH
     RLMGDFIPSP ETYQLLISKK INPSELNYKP YPFLLANTFD KKIIDKSIND FQFEWKWDGI
     RIQLIKRDGK ISIWSRGQEL VNKSFPELVE KIVFIKDDFV VDGELLVWNS IEDLPMNFSL
     LQKRLNRKEP SRKIQKSFPI TFIAYDLLEI DGEDQREFNL KNRRINLENN FYKWLNESEE
     DLSNIFKISK LIYPKNWKEA EMFKNNSRDN GTEGLVIKNK NSNYSPGRKK GLWWKYKVDP
     MQLDAVLIYA KGGTGIRAGL YTDYSFGLWK DGELIKFASA YSGLNNTEIK ELDKWIRQNT
     IERFGPVRSV KPKMVFEISF ENIQRSKRHK SGIAVRFPRI TKWRKDKFIQ DADTLENAQK
     LILSE
//